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Protein

tRNA(Ile)-lysidine synthase

Gene

tilS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This enzyme is essential for viability.

Catalytic activityi

(tRNA(Ile2))-cytidine(34) + L-lysine + ATP = (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H2O.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 256ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct
  • tRNA(Ile)-lysidine synthase activity Source: EcoCyc

GO - Biological processi

  • tRNA modification Source: EcoliWiki
  • wobble base lysidine biosynthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6096-MONOMER.
ECOL316407:JW0183-MONOMER.
MetaCyc:G6096-MONOMER.
BRENDAi6.3.4.19. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA(Ile)-lysidine synthase (EC:6.3.4.19)
Alternative name(s):
tRNA(Ile)-2-lysyl-cytidine synthase
tRNA(Ile)-lysidine synthetase
Gene namesi
Name:tilS
Synonyms:mesJ, yaeN
Ordered Locus Names:b0188, JW0183
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13220. tilS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432tRNA(Ile)-lysidine synthasePRO_0000181689Add
BLAST

Proteomic databases

PaxDbiP52097.
PRIDEiP52097.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-556745,EBI-556745

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261685. 154 interactions.
DIPiDIP-10190N.
IntActiP52097. 17 interactions.
MINTiMINT-1261006.
STRINGi511145.b0188.

Structurei

Secondary structure

432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 99Combined sources
Beta strandi13 – 186Combined sources
Helixi23 – 3614Combined sources
Beta strandi43 – 497Combined sources
Helixi57 – 7014Combined sources
Beta strandi75 – 784Combined sources
Beta strandi85 – 873Combined sources
Turni88 – 914Combined sources
Helixi92 – 10312Combined sources
Beta strandi109 – 1124Combined sources
Helixi117 – 12812Combined sources
Turni129 – 1313Combined sources
Helixi136 – 1383Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi149 – 1524Combined sources
Helixi154 – 1563Combined sources
Helixi160 – 16910Combined sources
Helixi180 – 1823Combined sources
Helixi186 – 1927Combined sources
Helixi194 – 2018Combined sources
Helixi205 – 23430Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2433Combined sources
Helixi244 – 2463Combined sources
Helixi251 – 26414Combined sources
Helixi272 – 28110Combined sources
Turni282 – 2843Combined sources
Helixi287 – 2893Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi298 – 31114Combined sources
Beta strandi320 – 3223Combined sources
Turni324 – 3274Combined sources
Beta strandi338 – 34710Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi364 – 3663Combined sources
Helixi377 – 3848Combined sources
Helixi388 – 3903Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi402 – 4065Combined sources
Turni407 – 4093Combined sources
Beta strandi410 – 4123Combined sources
Helixi413 – 4153Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi423 – 4286Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI5X-ray2.65A1-432[»]
ProteinModelPortaliP52097.
SMRiP52097. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52097.

Family & Domainsi

Domaini

The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.

Sequence similaritiesi

Belongs to the tRNA(Ile)-lysidine synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105D3U. Bacteria.
COG0037. LUCA.
HOGENOMiHOG000236507.
InParanoidiP52097.
KOiK04075.
OMAiDRNFLRQ.
OrthoDBiEOG6NKR0V.
PhylomeDBiP52097.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01161. tRNA_Ile_lys_synt.
InterProiIPR012796. Lysidine-tRNA-synth_C.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. TilS/TtcA_N.
IPR012094. tRNA_Ile_lys_synt.
IPR012795. tRNA_Ile_lys_synt_N.
IPR015262. tRNA_Ile_lys_synt_subst-bd.
[Graphical view]
PANTHERiPTHR11807:SF2. PTHR11807:SF2. 1 hit.
PfamiPF01171. ATP_bind_3. 1 hit.
PF09179. TilS. 1 hit.
PF11734. TilS_C. 1 hit.
[Graphical view]
SMARTiSM00977. TilS_C. 1 hit.
[Graphical view]
SUPFAMiSSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR02433. lysidine_TilS_C. 1 hit.
TIGR02432. lysidine_TilS_N. 1 hit.

Sequencei

Sequence statusi: Complete.

P52097-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GVALRAIHVH
60 70 80 90 100
HGLSANADAW VTHCENVCQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA
110 120 130 140 150
FARTLLPGEV LVTAQHLDDQ CETFLLALKR GSGPAGLSAM AEVSEFAGTR
160 170 180 190 200
LIRPLLARTR GELVQWARQY DLRWIEDESN QDDSYDRNFL RLRVVPLLQQ
210 220 230 240 250
RWPHFAEATA RSAALCAEQE SLLDELLADD LAHCQSPQGT LQIVPMLAMS
260 270 280 290 300
DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRLGAFEI
310 320 330 340 350
RRYQSQLWWI KSVTGQSENI VPWQTWLQPL ELPAGLGSVQ LNAGGDIRPP
360 370 380 390 400
RADEAVSVRF KAPGLLHIVG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG
410 420 430
ETLIAAAGVF VTQEGVAEGE NGVSFVWQKT LS
Length:432
Mass (Da):48,204
Last modified:October 1, 1996 - v1
Checksum:i26946DC7220B5A40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49445 Genomic DNA. Translation: BAA08428.1.
Z50870 Genomic DNA. Translation: CAA90751.1.
U70214 Genomic DNA. Translation: AAB08617.1.
U00096 Genomic DNA. Translation: AAC73299.1.
AP009048 Genomic DNA. Translation: BAA77863.1.
BR000032 Genomic DNA. Translation: FAA00003.1.
PIRiD64743.
RefSeqiNP_414730.1. NC_000913.3.
WP_000176549.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73299; AAC73299; b0188.
BAA77863; BAA77863; BAA77863.
GeneIDi944889.
KEGGiecj:JW0183.
eco:b0188.
PATRICi32115487. VBIEscCol129921_0195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49445 Genomic DNA. Translation: BAA08428.1.
Z50870 Genomic DNA. Translation: CAA90751.1.
U70214 Genomic DNA. Translation: AAB08617.1.
U00096 Genomic DNA. Translation: AAC73299.1.
AP009048 Genomic DNA. Translation: BAA77863.1.
BR000032 Genomic DNA. Translation: FAA00003.1.
PIRiD64743.
RefSeqiNP_414730.1. NC_000913.3.
WP_000176549.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI5X-ray2.65A1-432[»]
ProteinModelPortaliP52097.
SMRiP52097. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261685. 154 interactions.
DIPiDIP-10190N.
IntActiP52097. 17 interactions.
MINTiMINT-1261006.
STRINGi511145.b0188.

Proteomic databases

PaxDbiP52097.
PRIDEiP52097.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73299; AAC73299; b0188.
BAA77863; BAA77863; BAA77863.
GeneIDi944889.
KEGGiecj:JW0183.
eco:b0188.
PATRICi32115487. VBIEscCol129921_0195.

Organism-specific databases

EchoBASEiEB3011.
EcoGeneiEG13220. tilS.

Phylogenomic databases

eggNOGiENOG4105D3U. Bacteria.
COG0037. LUCA.
HOGENOMiHOG000236507.
InParanoidiP52097.
KOiK04075.
OMAiDRNFLRQ.
OrthoDBiEOG6NKR0V.
PhylomeDBiP52097.

Enzyme and pathway databases

BioCyciEcoCyc:G6096-MONOMER.
ECOL316407:JW0183-MONOMER.
MetaCyc:G6096-MONOMER.
BRENDAi6.3.4.19. 2026.

Miscellaneous databases

EvolutionaryTraceiP52097.
PROiP52097.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01161. tRNA_Ile_lys_synt.
InterProiIPR012796. Lysidine-tRNA-synth_C.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. TilS/TtcA_N.
IPR012094. tRNA_Ile_lys_synt.
IPR012795. tRNA_Ile_lys_synt_N.
IPR015262. tRNA_Ile_lys_synt_subst-bd.
[Graphical view]
PANTHERiPTHR11807:SF2. PTHR11807:SF2. 1 hit.
PfamiPF01171. ATP_bind_3. 1 hit.
PF09179. TilS. 1 hit.
PF11734. TilS_C. 1 hit.
[Graphical view]
SMARTiSM00977. TilS_C. 1 hit.
[Graphical view]
SUPFAMiSSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR02433. lysidine_TilS_C. 1 hit.
TIGR02432. lysidine_TilS_N. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Yamamoto Y.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "An Escherichia coli gene (yaeO) suppresses temperature-sensitive mutations in essential genes by modulating Rho-dependent transcription termination."
    Pichoff S., Alibaud L., Guedant A., Castanie M.-P., Bouche J.-P.
    Mol. Microbiol. 29:859-869(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA."
    Soma A., Ikeuchi Y., Kanemasa S., Kobayashi K., Ogasawara N., Ote T., Kato J., Watanabe K., Sekine Y., Suzuki T.
    Mol. Cell 12:689-698(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, CHARACTERIZATION.
  8. "Structure of the MesJ Pp-ATPase from Escherichia coli."
    Gu M., Burling T., Lima C.D.
    Submitted (JAN-2003) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiTILS_ECOLI
AccessioniPrimary (citable) accession number: P52097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 13, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.